The domain within your query sequence starts at position 133 and ends at position 183; the E-value for the CTLH domain shown below is 6e-28.
EHPSATKFRNHVMEGDWDKAENDLNELKPLVHSPHAIVAQTFSETSSNFFP
The domain was found using the schnipsel database
CTLHC-terminal to LisH motif. |
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SMART accession number: | SM00668 |
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Description: | Alpha-helical motif of unknown function. |
Interpro abstract (IPR006595): | The 33-residue LIS1 homology (LisH) motif ( IPR006594 ) is found in eukaryotic intracellular proteins involved in microtubule dynamics, cell migration, nucleokinesis and chromosome segregation. The LisH motif is likely to possess a conserved protein-binding function and it has been proposed that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerization, or else by binding cytoplasmic dynein heavy chain or microtubules directly. The LisH motif is found associated to other domains, such as WD-40 SPRY, Kelch, AAA ATPase, RasGEF, or HEAT [ (PUBMED:11734546) (PUBMED:12384287) (PUBMED:12559565) ]. The secondary structure of the LisH domain is predicted to be two alpha- helices [ (PUBMED:11734546) ]. Some proteins known to contain a LisH motif are listed below:
The C-terminal to LisH (CTLH) motif is a predicted alpha-helical sequence of unknown function that is found adjacent to the LisH motif in a number of these proteins but is absent in other (e.g. LIS1) [ (PUBMED:11734546) (PUBMED:12384287) (PUBMED:12559565) ]. The CTLH domain can also be found in the absence of the LisH motif, like in:
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Family alignment: |
There are 10212 CTLH domains in 10020 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
- Cellular role (predicted cellular role)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)